ArticleNucleic acids research2015
Partitioning between recoding and termination at a stop codon-selenocysteine insertion sequence.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Stop codon reassignment to tryptophan in members of the bacterial phylumMicrobial genomics · 2026Article
- Modulation of protein activity by small RNA base pairing internal to coding sequences.Molecular cell · 2025Article
- Genetic Determinants of Selenium Availability, Selenium-Response, and Risk of Polycystic Ovary Syndrome.Biological trace element research · 2024Article
- Modifications in the T arm of tRNA globally determine tRNA maturation, function, and cellular fitness.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon.Science (New York, N.Y.) · 2022Article
- Mechanisms Affecting the Biosynthesis and Incorporation Rate of Selenocysteine.Molecules (Basel, Switzerland) · 2021Review
- Analysis of Stop Codons within Prokaryotic Protein-Coding Genes Suggests Frequent Readthrough Events.International journal of molecular sciences · 2021Article
- Translational recoding: canonical translation mechanisms reinterpreted.Nucleic acids research · 2020Review
- The Selenium Transport Protein, Selenoprotein P, Requires Coding Sequence Determinants to Promote Efficient Selenocysteine Incorporation.Journal of molecular biology · 2018Article
- On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins.Biochimica et biophysica acta. General subjects · 2018Review
- Roles of elusive translational GTPases come to light and inform on the process of ribosome biogenesis in bacteria.Molecular microbiology · 2018Review
- Ribosome dynamics during decoding.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Article
- Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.Nature communications · 2016Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selenocysteine (Sec) is inserted into proteins by recoding a UGA stop codon followed by a selenocysteine insertion sequence (SECIS). UGA recoding by the Sec machinery is believed to be very inefficient owing to RF2-mediated termination at UGA. Here we show that recoding efficiency in vivo is 30-40% independently of the cell growth rate. Efficient recoding requires sufficient selenium concentrations in the medium. RF2 is an unexpectedly poor competitor of Sec. We recapitulate the major characteristics of SECIS-dependent UGA recoding in vitro using a fragment of fdhF-mRNA encoding a natural bacterial selenoprotein. Only 40% of actively translating ribosomes that reach the UGA codon insert Sec, even in the absence of RF2, suggesting that the capacity to insert Sec into proteins is inherently limited. RF2 does not compete with the Sec incorporation machinery; rather, it terminates translation on those ribosomes that failed to incorporate Sec. The data suggest a model in which early recruitment of Sec-tRNA(Sec)-SelB-GTP to the SECIS blocks the access of RF2 to the stop codon, thereby prioritizing recoding over termination at Sec-dedicated stop codons.
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